8fab: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:8fab.gif|left|200px]]
{{Seed}}
[[Image:8fab.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_8fab|  PDB=8fab  |  SCENE=  }}  
{{STRUCTURE_8fab|  PDB=8fab  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION'''
===CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION===




==Overview==
<!--
The structure of the antigen-binding fragment (Fab) of an anti-p-azophenylarsonate monoclonal antibody, 36-71, bearing a major cross-reactive idiotype of A/J mice has been refined to an R factor of 24.8% at a resolution of 1.85 A. The previously solved partial structure of this Fab at a resolution of 2.9 A (Rose et al., 1990) was used as an initial model for refinement against the high-resolution data. The complex with hapten has been modeled by docking the small-molecule crystal structure of phenylarsonic acid into the structure of the native Fab on the basis of a low-resolution electron density map of the complex. In this model, residue Arg-96 in the light chain and residues Asn-35, Trp-47, and Ser-99 in the heavy chain contact the arsonate moiety of the hapten; an additional bond is found between the arsonate group and a tightly bound water molecule. The phenyl moiety of the hapten packs against two tyrosine side chains at positions 50 and 106 in the heavy chain. Residue Arg-96 in the light chain had been implicated as involved in hapten binding on the basis of previous experiments, and indeed, this residue appears to play a crucial role in this model. Experiments employing site-directed mutagenesis directly support this conclusion. The heavy-chain complementarity-determining regions have novel conformations not previously observed in immunoglobulins except for the recently solved anti-p-azophenylarsonate Fab R 19.9 (Lascombe et al., 1989).
The line below this paragraph, {{ABSTRACT_PUBMED_2015229}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 2015229 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_2015229}}


==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Saul, F A.]]
[[Category: Saul, F A.]]
[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:49:16 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 12:57:58 2008''

Revision as of 09:57, 11 July 2008

File:8fab.png

Template:STRUCTURE 8fab

CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 2015229

About this Structure

8FAB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten., Strong RK, Campbell R, Rose DR, Petsko GA, Sharon J, Margolies MN, Biochemistry. 1991 Apr 16;30(15):3739-48. PMID:2015229

Page seeded by OCA on Fri Jul 11 12:57:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=8fab&oldid=639304"